scholarly journals Structural Property of Decorin from Small Intestine and its Effect of Type I Collagen Fibril Formation

1998 ◽  
Vol 69 (8) ◽  
pp. 779-791
Author(s):  
Yoshihiro NOMURA ◽  
Takahiro MIZUTANI ◽  
Yasuhiro ISHII ◽  
Kunio SHIRAI
Keyword(s):  
Small Intestine ◽  
Structural Property ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals The Mammalian Chitinase-like Lectin, YKL-40, Binds Specifically to Type I Collagen and Modulates the Rate of Type I Collagen Fibril Formation

2006 ◽  
Vol 281 (30) ◽  
pp. 21082-21095 ◽  
Author(s):  
Heather F. Bigg ◽  
Robin Wait ◽  
Andrew D. Rowan ◽  
Tim E. Cawston
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals Osteopontin regulates type I collagen fibril formation in bone tissue

2020 ◽  
Author(s):  
Baptiste Depalle ◽  
Catriona M. McGilvery ◽  
Sabah Nobakhti ◽  
Nouf Aldegaither ◽  
Sandra J. Shefelbine ◽  
...  
Keyword(s):  
Bone Tissue ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Effect of UV irradiation on type I collagen fibril formation in neutral collagen solutions

2001 ◽  
Vol 17 (3) ◽  
pp. 114-120 ◽  
Author(s):  
Julian M. Menter ◽  
Abrienne M. Patta ◽  
Robert M. Sayre ◽  
John Dowdy ◽  
Isaac Willis
Keyword(s):  
Uv Irradiation ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Characterization of Type I Collagen Fibril Formation Using Thioflavin T Fluorescent Dye

2009 ◽  
Vol 145 (5) ◽  
pp. 677-684 ◽  
Author(s):  
K. Morimoto ◽  
K. Kawabata ◽  
S. Kunii ◽  
K. Hamano ◽  
T. Saito ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Fluorescent Dye ◽  
Thioflavin T ◽  
Type I

scholarly journals Structure–function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro

2000 ◽  
Vol 349 (3) ◽  
pp. 877-883 ◽  
Author(s):  
Christy A. THOMSON ◽  
Vettai S. ANANTHANARAYANAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Molar Ratio ◽  
Functional Assay ◽  
Type I ◽  
Ph Dependent ◽  
Ph Range

Hsp47, a 47kDa heat shock protein whose expression level parallels that of collagen, has been regarded as a collagen-specific molecular chaperone. Studies from other laboratories have established the association of Hsp47 with the nascent as well as the triple-helical procollagen molecule in the endoplasmic reticulum and its dissociation from procollagen in the Golgi. One of several roles suggested for Hsp47 in collagen biosynthesis is the prevention of aggregation of procollagen in the endoplasmic reticulum. However, no experimental evidence has been available to verify this suggestion. In the present study we have followed the aggregation of mature triple-helical collagen molecules into fibrils by using turbidimetric measurements in the absence and presence of Hsp47. In the pH range 6–7, fibril formation of type I collagen, as monitored by turbidimetry, proceeds with a lag of approx. 10min and levels off by approx. 60min. The addition of Hsp47 at pH 7 effectively inhibits fibril formation at and above a 1:1 molar ratio of Hsp47 to triple-helical collagen. This inhibition is markedly pH-dependent, being significantly diminished at pH 6. CD and fluorescence spectral data of Hsp47 in the pH range 4.2–7.4 reveal a significant alteration in its structure at pH values below 6.2, with a decrease in α-helix and an increase in β-structure. This conformational change is likely to be the basis of the decreased binding of Hsp47 to collagen in vitro at pH 6.3 as well as its inability to inhibit collagen fibril formation at this pH. Our results also provide a functional assay for Hsp47 that can be used in studies on collagen and Hsp47 interactions.

scholarly journals Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

2010 ◽  
Vol 285 (23) ◽  
pp. 17465-17470 ◽  
Author(s):  
Saori Kunii ◽  
Koichi Morimoto ◽  
Kouhei Nagai ◽  
Takuya Saito ◽  
Kenji Sato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals Temperature-Responsive Gelation of Type I Collagen Solutions Involving Fibril Formation and Genipin Crosslinking as a Potential Injectable Hydrogel

2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Shunji Yunoki ◽  
Yoshimi Ohyabu ◽  
Hirosuke Hatayama
Keyword(s):  
Room Temperature ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I ◽  
Temperature Responsive ◽  
Moderate Change ◽  
Living Tissues ◽  
Cell Carriers ◽  
Temperature Responses ◽  
Gel System

We investigated the temperature-responsive gelation of collagen/genipin solutions using pepsin-solubilized collagen (PSC) and acid-solubilized collagen (ASC) as substrates. Gelation occurred in the PSC/genipin solutions at genipin concentrations 0–2 mM under moderate change in temperature from 25 to 37°C. The PSC/genipin solutions exhibited fluidity at room temperature for at least 30 min, whereas the ASC/genipin solutions rapidly reached gel points. In specific cases PSC would be preferred over ASC as an injectable gel system. The temperature-responsive gelation of PSC/genipin solutions was due to temperature responses to genipin crosslinking and collagen fibril formation. The elastic modulus of the 0.5% PSC/genipin gel system could be adjusted in a range of 2.5 to 50 kPa by the PSC and genipin concentrations, suggesting that a PSC/genipin solution is a potential injectable gel system for drug and cell carriers, with mechanical properties matching those of living tissues.

scholarly journals Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis

2006 ◽  
Vol 17 (5) ◽  
pp. 2346-2355 ◽  
Author(s):  
Yoshihito Ishida ◽  
Hiroshi Kubota ◽  
Akitsugu Yamamoto ◽  
Akira Kitamura ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Type I Collagen ◽  
Intracellular Localization ◽  
Fibril Formation ◽  
Mouse Embryos ◽  
Type I ◽  
Collagen Types ◽  
Protease Digestion ◽  
Triple Helices ◽  
Increased Susceptibility

Heat-shock protein of 47 kDa (Hsp47) is a molecular chaperone that recognizes collagen triple helices in the endoplasmic reticulum (ER). Hsp47-knockout mouse embryos are deficient in the maturation of collagen types I and IV, and collagen triple helices formed in the absence of Hsp47 show increased susceptibility to protease digestion. We show here that the fibrils of type I collagen produced by Hsp47-/- cells are abnormally thin and frequently branched. Type I collagen was highly accumulated in the ER of Hsp47-/- cells, and its secretion rate was much slower than that of Hsp47+/+ cells, leading to accumulation of the insoluble aggregate of type I collagen within the cells. Transient expression of Hsp47 in the Hsp47-/- cells restored normal extracellular fibril formation and intracellular localization of type I collagen. Intriguingly, type I collagen with unprocessed N-terminal propeptide (N-propeptide) was secreted from Hsp47-/- cells and accumulated in the extracellular matrix. These results indicate that Hsp47 is required for correct folding and prevention of aggregation of type I collagen in the ER and that this function is indispensable for efficient secretion, processing, and fibril formation of collagen.

scholarly journals Matrix fully loaded: Assembly and secretion of collagen fibrils

2003 ◽  
Vol 25 (5) ◽  
pp. 11-13
Author(s):  
Karl E. Kadler ◽  
Elizabeth G. Canty ◽  
Yinhui Lu
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Secretory Pathway ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Collagen Fibrils ◽  
Type I ◽  
Small Proteins ◽  
Unpublished Work ◽  
Structural Work

The secretory pathway operates like a well-oiled machine when it comes to secreting small proteins. But how does it cope with stiff rod-like molecules such as type I collagen, which spontaneously self-assembles into the millimetre-long collagen fibrils that are characteristic of the extracellular matrix (ECM)? A recent study in our laboratory shows that the secretory pathway adapts exquisitely to intracellular fibril formation by creating tubular vesicles that dock to specialized secretory nozzles in the plasma membrane (E.G. Canty, Y. Lu, R.M. Meadows, M. Shaw, D.F. Holmes and K.E. Kadler, unpublished work). This article gives a brief account of the biochemical and structural work that led up to these new observations.

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